ATPF_ECOLI
ID ATPF_ECOLI Reviewed; 156 AA.
AC P0ABA0; P00859; Q2M854;
DT 21-JUL-1986, integrated into UniProtKB/Swiss-Prot.
DT 21-JUL-1986, sequence version 1.
DT 03-AUG-2022, entry version 129.
DE RecName: Full=ATP synthase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATP synthase F(0) sector subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=ATPase subunit I {ECO:0000255|HAMAP-Rule:MF_01398};
DE AltName: Full=F-type ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
DE Short=F-ATPase subunit b {ECO:0000255|HAMAP-Rule:MF_01398};
GN Name=atpF {ECO:0000255|HAMAP-Rule:MF_01398}; Synonyms=papF, uncF;
GN OrderedLocusNames=b3736, JW3714;
OS Escherichia coli (strain K12).
OC Bacteria; Proteobacteria; Gammaproteobacteria; Enterobacterales;
OC Enterobacteriaceae; Escherichia.
OX NCBI_TaxID=83333;
RN [1]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6395859; DOI=10.1042/bj2240799;
RA Walker J.E., Gay N.J., Saraste M., Eberle A.N.;
RT "DNA sequence around the Escherichia coli unc operon. Completion of the
RT sequence of a 17 kilobase segment containing asnA, oriC, unc, glmS and
RT phoS.";
RL Biochem. J. 224:799-815(1984).
RN [2]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6272190; DOI=10.1093/nar/9.16.3919;
RA Gay N.J., Walker J.E.;
RT "The atp operon: nucleotide sequence of the promoter and the genes for the
RT membrane proteins, and the delta subunit of Escherichia coli ATP-
RT synthase.";
RL Nucleic Acids Res. 9:3919-3926(1981).
RN [3]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6277311; DOI=10.1016/0006-291x(81)90495-2;
RA Kanazawa H., Mabuchi K., Kayano T., Noumi T., Sekiya T., Futai M.;
RT "Nucleotide sequence of the genes for F0 components of the proton-
RT translocating ATPase from Escherichia coli: prediction of the primary
RT structure of F0 subunits.";
RL Biochem. Biophys. Res. Commun. 103:613-620(1981).
RN [4]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6278247; DOI=10.1007/bf00271191;
RA Nielsen J., Hansen F.G., Hoppe J., Friedl P., von Meyenburg K.;
RT "The nucleotide sequence of the atp genes coding for the F0 subunits a, b,
RT c and the F1 subunit delta of the membrane bound ATP synthase of
RT Escherichia coli.";
RL Mol. Gen. Genet. 184:33-39(1981).
RN [5]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=6301339; DOI=10.1111/j.1749-6632.1982.tb25731.x;
RA Kanazawa H., Futai M.;
RT "Structure and function of H+-ATPase: what we have learned from Escherichia
RT coli H+-ATPase.";
RL Ann. N. Y. Acad. Sci. 402:45-64(1982).
RN [6]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA].
RX PubMed=2861200; DOI=10.1016/s0021-9258(17)39579-0;
RA Porter A.C.G., Kumamoto C., Aldape K., Simoni R.D.;
RT "Role of the b subunit of the Escherichia coli proton-translocating ATPase.
RT A mutagenic analysis.";
RL J. Biol. Chem. 260:8182-8187(1985).
RN [7]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=7686882; DOI=10.1006/geno.1993.1230;
RA Burland V.D., Plunkett G. III, Daniels D.L., Blattner F.R.;
RT "DNA sequence and analysis of 136 kilobases of the Escherichia coli genome:
RT organizational symmetry around the origin of replication.";
RL Genomics 16:551-561(1993).
RN [8]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / MG1655 / ATCC 47076;
RX PubMed=9278503; DOI=10.1126/science.277.5331.1453;
RA Blattner F.R., Plunkett G. III, Bloch C.A., Perna N.T., Burland V.,
RA Riley M., Collado-Vides J., Glasner J.D., Rode C.K., Mayhew G.F.,
RA Gregor J., Davis N.W., Kirkpatrick H.A., Goeden M.A., Rose D.J., Mau B.,
RA Shao Y.;
RT "The complete genome sequence of Escherichia coli K-12.";
RL Science 277:1453-1462(1997).
RN [9]
RP NUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA].
RC STRAIN=K12 / W3110 / ATCC 27325 / DSM 5911;
RX PubMed=16738553; DOI=10.1038/msb4100049;
RA Hayashi K., Morooka N., Yamamoto Y., Fujita K., Isono K., Choi S.,
RA Ohtsubo E., Baba T., Wanner B.L., Mori H., Horiuchi T.;
RT "Highly accurate genome sequences of Escherichia coli K-12 strains MG1655
RT and W3110.";
RL Mol. Syst. Biol. 2:E1-E5(2006).
RN [10]
RP NUCLEOTIDE SEQUENCE [GENOMIC DNA] OF 132-156.
RX PubMed=6458296; DOI=10.1016/0006-291x(81)91504-7;
RA Mabuchi K., Kanazawa H., Kayano T., Futai M.;
RT "Nucleotide sequence of the gene coding for the delta subunit of proton
RT translocating ATPase of Escherichia coli.";
RL Biochem. Biophys. Res. Commun. 102:172-179(1981).
RN [11]
RP FUNCTION.
RX PubMed=1682301; DOI=10.1128/jb.173.22.7240-7248.1991;
RA McCormick K.A., Cain B.D.;
RT "Targeted mutagenesis of the b subunit of F1F0 ATP synthase in Escherichia
RT coli: Glu-77 through Gln-85.";
RL J. Bacteriol. 173:7240-7248(1991).
RN [12]
RP SUBUNIT, AND SUBCELLULAR LOCATION.
RC STRAIN=BL21-DE3;
RX PubMed=16079137; DOI=10.1074/jbc.m506479200;
RA Stenberg F., Chovanec P., Maslen S.L., Robinson C.V., Ilag L.,
RA von Heijne G., Daley D.O.;
RT "Protein complexes of the Escherichia coli cell envelope.";
RL J. Biol. Chem. 280:34409-34419(2005).
RN [13]
RP STRUCTURE BY NMR OF 1-34.
RX PubMed=10336456; DOI=10.1074/jbc.274.22.15598;
RA Dmitriev O., Jones P.C., Jiang W., Fillingame R.H.;
RT "Structure of the membrane domain of subunit b of the Escherichia coli F0F1
RT ATP synthase.";
RL J. Biol. Chem. 274:15598-15604(1999).
CC -!- FUNCTION: F(1)F(0) ATP synthase produces ATP from ADP in the presence
CC of a proton or sodium gradient. F-type ATPases consist of two
CC structural domains, F(1) containing the extramembraneous catalytic core
CC and F(0) containing the membrane proton channel, linked together by a
CC central stalk and a peripheral stalk. During catalysis, ATP synthesis
CC in the catalytic domain of F(1) is coupled via a rotary mechanism of
CC the central stalk subunits to proton translocation. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- FUNCTION: Component of the F(0) channel, it forms part of the
CC peripheral stalk, linking F(1) to F(0). {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- SUBUNIT: F-type ATPases have 2 components, F(1) - the catalytic core
CC - and F(0) - the membrane proton channel. F(1) has five subunits:
CC alpha(3), beta(3), gamma(1), delta(1), epsilon(1). F(0) has three main
CC subunits: a(1), b(2) and c(10-14). The alpha and beta chains form an
CC alternating ring which encloses part of the gamma chain. F(1) is
CC attached to F(0) by a central stalk formed by the gamma and epsilon
CC chains, while a peripheral stalk is formed by the delta and b chains.
CC {ECO:0000255|HAMAP-Rule:MF_01398}.
CC -!- SUBCELLULAR LOCATION: Cell inner membrane {ECO:0000255|HAMAP-
CC Rule:MF_01398}; Single-pass membrane protein {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
CC -!- SIMILARITY: Belongs to the ATPase B chain family. {ECO:0000255|HAMAP-
CC Rule:MF_01398}.
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DR EMBL; J01594; AAA24733.1; -; Genomic_DNA.
DR EMBL; X01631; CAA25778.1; -; Genomic_DNA.
DR EMBL; V00264; CAA23516.1; -; Genomic_DNA.
DR EMBL; V00310; CAA23592.1; -; Genomic_DNA.
DR EMBL; V00266; CAA23523.1; -; Genomic_DNA.
DR EMBL; M25464; AAA83871.1; -; Genomic_DNA.
DR EMBL; M10422; AAA24741.1; -; Genomic_DNA.
DR EMBL; L10328; AAA62088.1; -; Genomic_DNA.
DR EMBL; U00096; AAC76759.1; -; Genomic_DNA.
DR EMBL; AP009048; BAE77552.1; -; Genomic_DNA.
DR EMBL; M12212; AAA20043.1; -; Unassigned_DNA.
DR PIR; D93732; LWECB.
DR RefSeq; NP_418192.1; NC_000913.3.
DR RefSeq; WP_001052219.1; NZ_STEB01000015.1.
DR PDB; 1B9U; NMR; -; A=1-34.
DR PDB; 1L2P; X-ray; 1.55 A; A=62-122.
DR PDB; 2KHK; NMR; -; A=30-82.
DR PDB; 5T4O; EM; 6.90 A; I/J=2-156.
DR PDB; 5T4P; EM; 7.77 A; I/J=2-156.
DR PDB; 5T4Q; EM; 8.53 A; I/J=2-156.
DR PDB; 6OQR; EM; 3.10 A; X/Y=1-156.
DR PDB; 6OQS; EM; 3.30 A; X/Y=1-156.
DR PDB; 6OQT; EM; 3.10 A; X/Y=1-156.
DR PDB; 6OQU; EM; 3.20 A; X/Y=1-156.
DR PDB; 6OQV; EM; 3.30 A; X/Y=1-156.
DR PDB; 6OQW; EM; 3.10 A; X/Y=1-156.
DR PDB; 6PQV; EM; 3.30 A; X/Y=1-156.
DR PDB; 6VWK; EM; 3.30 A; X/Y=1-156.
DR PDB; 6WNQ; EM; 3.40 A; X/Y=1-156.
DR PDB; 6WNR; EM; 3.30 A; X/Y=1-156.
DR PDBsum; 1B9U; -.
DR PDBsum; 1L2P; -.
DR PDBsum; 2KHK; -.
DR PDBsum; 5T4O; -.
DR PDBsum; 5T4P; -.
DR PDBsum; 5T4Q; -.
DR PDBsum; 6OQR; -.
DR PDBsum; 6OQS; -.
DR PDBsum; 6OQT; -.
DR PDBsum; 6OQU; -.
DR PDBsum; 6OQV; -.
DR PDBsum; 6OQW; -.
DR PDBsum; 6PQV; -.
DR PDBsum; 6VWK; -.
DR PDBsum; 6WNQ; -.
DR PDBsum; 6WNR; -.
DR AlphaFoldDB; P0ABA0; -.
DR SMR; P0ABA0; -.
DR BioGRID; 4262109; 80.
DR ComplexPortal; CPX-4022; ATP synthase complex.
DR DIP; DIP-35994N; -.
DR IntAct; P0ABA0; 2.
DR STRING; 511145.b3736; -.
DR DrugBank; DB03091; Isoglutamine.
DR TCDB; 3.A.2.1.1; the h(+)- or na(+)-translocating f-type, v-type and a-type atpase (f-atpase) superfamily.
DR SWISS-2DPAGE; P0ABA0; -.
DR jPOST; P0ABA0; -.
DR PaxDb; P0ABA0; -.
DR PRIDE; P0ABA0; -.
DR EnsemblBacteria; AAC76759; AAC76759; b3736.
DR EnsemblBacteria; BAE77552; BAE77552; BAE77552.
DR GeneID; 67417723; -.
DR GeneID; 948247; -.
DR KEGG; ecj:JW3714; -.
DR KEGG; eco:b3736; -.
DR PATRIC; fig|1411691.4.peg.2964; -.
DR EchoBASE; EB0101; -.
DR eggNOG; COG0711; Bacteria.
DR HOGENOM; CLU_079215_4_5_6; -.
DR InParanoid; P0ABA0; -.
DR OMA; FAWKPIL; -.
DR PhylomeDB; P0ABA0; -.
DR BioCyc; EcoCyc:ATPF-MON; -.
DR BioCyc; MetaCyc:ATPF-MON; -.
DR EvolutionaryTrace; P0ABA0; -.
DR PRO; PR:P0ABA0; -.
DR Proteomes; UP000000318; Chromosome.
DR Proteomes; UP000000625; Chromosome.
DR GO; GO:0016021; C:integral component of membrane; IEA:UniProtKB-KW.
DR GO; GO:0005886; C:plasma membrane; IC:ComplexPortal.
DR GO; GO:0045259; C:proton-transporting ATP synthase complex; IPI:ComplexPortal.
DR GO; GO:0045263; C:proton-transporting ATP synthase complex, coupling factor F(o); IMP:EcoliWiki.
DR GO; GO:0046933; F:proton-transporting ATP synthase activity, rotational mechanism; IMP:EcoCyc.
DR GO; GO:0046961; F:proton-transporting ATPase activity, rotational mechanism; IMP:EcoCyc.
DR GO; GO:0042777; P:proton motive force-driven plasma membrane ATP synthesis; IMP:ComplexPortal.
DR HAMAP; MF_01398; ATP_synth_b_bprime; 1.
DR InterPro; IPR028987; ATP_synth_B-like_membr_sf.
DR InterPro; IPR002146; ATP_synth_b/b'su_bac/chlpt.
DR InterPro; IPR005864; ATP_synth_F0_bsu_bac.
DR Pfam; PF00430; ATP-synt_B; 1.
DR SUPFAM; SSF81573; SSF81573; 1.
DR TIGRFAMs; TIGR01144; ATP_synt_b; 1.
PE 1: Evidence at protein level;
KW 3D-structure; ATP synthesis; Cell inner membrane; Cell membrane; CF(0);
KW Hydrogen ion transport; Ion transport; Membrane; Reference proteome;
KW Transmembrane; Transmembrane helix; Transport.
FT CHAIN 1..156
FT /note="ATP synthase subunit b"
FT /id="PRO_0000082371"
FT TRANSMEM 11..31
FT /note="Helical"
FT /evidence="ECO:0000255|HAMAP-Rule:MF_01398"
FT SITE 9
FT /note="Mutation prevents the formation of a functional
FT proton pore, but has a small effect on the binding of F(1)
FT to F(0)"
FT SITE 131
FT /note="Required for proton pore formation, as well as F(1)
FT to F(0) binding"
FT CONFLICT 33
FT /note="I -> F (in Ref. 3; CAA23592)"
FT /evidence="ECO:0000305"
FT CONFLICT 62
FT /note="T -> N (in Ref. 7; AAA24741)"
FT /evidence="ECO:0000305"
FT CONFLICT 72
FT /note="A -> D (in Ref. 3; CAA23592)"
FT /evidence="ECO:0000305"
FT HELIX 6..24
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 26..41
FT /evidence="ECO:0007829|PDB:6OQV"
FT HELIX 44..48
FT /evidence="ECO:0007829|PDB:6OQV"
FT HELIX 63..120
FT /evidence="ECO:0007829|PDB:1L2P"
FT STRAND 136..138
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 143..145
FT /evidence="ECO:0007829|PDB:6OQR"
FT HELIX 146..154
FT /evidence="ECO:0007829|PDB:6OQR"
SQ SEQUENCE 156 AA; 17264 MW; 51A93C8BEE9AD9DF CRC64;
MNLNATILGQ AIAFVLFVLF CMKYVWPPLM AAIEKRQKEI ADGLASAERA HKDLDLAKAS
ATDQLKKAKA EAQVIIEQAN KRRSQILDEA KAEAEQERTK IVAQAQAEIE AERKRAREEL
RKQVAILAVA GAEKIIERSV DEAANSDIVD KLVAEL
